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Updated: May 27, 2026

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance

Published on: January 3, 2012

Heat-labile enterotoxin: beyond G(m1) binding.

Benjamin Mudrak¹, Meta J Kuehn

¹Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC 27710, USA. bm36@duke.edu

|November 10, 2011

Summary

Enterotoxigenic Escherichia coli (ETEC) causes significant global illness. This review details the heat-labile enterotoxin (LT) B-subunit

Area of Science:

Microbiology
Molecular Biology
Toxicology

Background:

Enterotoxigenic Escherichia coli (ETEC) is a major cause of diarrheal disease globally.
Heat-labile enterotoxin (LT) is a key virulence factor produced by ETEC, structurally and functionally resembling cholera toxin.
LT comprises a single A subunit and a pentameric B subunit (LTB).

Purpose of the Study:

To review the regulation, assembly, and binding characteristics of the LT B-subunit pentamer.
To explore the diverse molecular interactions of the LTB subunit.
To elucidate the role of LTB in ETEC pathogenesis.

Main Methods:

Literature review of studies on ETEC and LT.
Analysis of structural and functional data of the LT B-subunit.

Keywords:

ETEC GM1 blood antigen heat-labile enterotoxin lipopolysaccharide

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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

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Last Updated: May 27, 2026

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance

Published on: January 3, 2012

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Examination of host-pathogen interaction mechanisms.

Main Results:

LTB binds the host receptor monosialoganglioside G(M1).
Recent findings highlight additional interactions with A-type blood sugars and E. coli lipopolysaccharide.
The LTB pentamer exhibits complex binding properties influencing toxin activity.

Conclusions:

Understanding LTB's interactions is crucial for comprehending ETEC virulence.
Further research into these molecular interactions may reveal novel therapeutic targets.
The multifaceted binding of LTB underscores its importance in ETEC pathogenesis.